S11 Table provides the total number of nsSNVs affecting post-translational modification of amino acids. In the gene TNN, cancer-associated nsSNVs within HERV elements were found to likely impact amino acid post-translational modification (PTM) sites that led to phosphorylation gain or loss. In KIR2DL1, mutations were found to likely impact multiple functions such as phosphorylation, glycosylation, and ligand binding site. In OR4K15 and ZNF99, nsSNVs affect the modification of amino acid phosphorylation and glycosylation. Here, OR4K15 is linked to cancer.